Variations of ecdysone titer and hemolymph major proteins during the molt cycle of the spider crab Acanthonyx lunulatus

Abstract

1. 1. Two dimensional electrophoresis (IEF-SDS) of the spider crab Acanthonyx lunulatus hemolymph shows the presence of four polypeptide AL 1 (molecular weight 74,000), AL 2 (76,000), AL 3 (81,000) and AL 4 (84,000). This method allows a rapid and reproducible characterization of hemolymph proteins. 2. 2. When hemocyanin is purified by high speed centrifugations the resulting pellet contains the same four polypeptides showing that hemocyanin is the major component of the hemolymph of Acanthonyx lunulatus. 3. 3. Qualitative changes in hemolymph protein associated with molting has been demonstrated by IEF-SDS: a new polypeptide AL 5 (88,000) different from protein AL 1, AL 2, AL 3 and AL 4 (as shown by the limited proteolysis technique of Cleveland, 1977) is present at stages D 0, D 1, D 2 D 3. This protein appears in hemolymph when the ecdysone titer increases.